NU107_DROME
ID NU107_DROME Reviewed; 845 AA.
AC Q9V466;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Nuclear pore complex protein Nup107 {ECO:0000305};
DE AltName: Full=Nucleoporin Nup107 {ECO:0000305};
GN Name=Nup107 {ECO:0000312|FlyBase:FBgn0027868};
GN ORFNames=CG6743 {ECO:0000312|FlyBase:FBgn0027868};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAD46878.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD46878.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAD46878.1};
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18562695; DOI=10.1091/mbc.e07-11-1162;
RA Katsani K.R., Karess R.E., Dostatni N., Doye V.;
RT "In vivo dynamics of Drosophila nuclear envelope components.";
RL Mol. Biol. Cell 19:3652-3666(2008).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-364.
RX PubMed=26485283; DOI=10.1172/jci83553;
RA Weinberg-Shukron A., Renbaum P., Kalifa R., Zeligson S., Ben-Neriah Z.,
RA Dreifuss A., Abu-Rayyan A., Maatuk N., Fardian N., Rekler D., Kanaan M.,
RA Samson A.O., Levy-Lahad E., Gerlitz O., Zangen D.;
RT "A mutation in the nucleoporin-107 gene causes XX gonadal dysgenesis.";
RL J. Clin. Invest. 125:4295-4304(2015).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26502056; DOI=10.1038/ncb3258;
RA Ryu T., Spatola B., Delabaere L., Bowlin K., Hopp H., Kunitake R.,
RA Karpen G.H., Chiolo I.;
RT "Heterochromatic breaks move to the nuclear periphery to continue
RT recombinational repair.";
RL Nat. Cell Biol. 17:1401-1411(2015).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27402967; DOI=10.1242/bio.017566;
RA Hayashi D., Tanabe K., Katsube H., Inoue Y.H.;
RT "B-type nuclear lamin and the nuclear pore complex Nup107-160 influences
RT maintenance of the spindle envelope required for cytokinesis in Drosophila
RT male meiosis.";
RL Biol. Open 5:1011-1021(2016).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=31626769; DOI=10.1016/j.cell.2019.09.022;
RA Hampoelz B., Schwarz A., Ronchi P., Bragulat-Teixidor H., Tischer C.,
RA Gaspar I., Ephrussi A., Schwab Y., Beck M.;
RT "Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.";
RL Cell 179:671-686.E17(2019).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31784359; DOI=10.1016/j.molcel.2019.10.017;
RA Gozalo A., Duke A., Lan Y., Pascual-Garcia P., Talamas J.A., Nguyen S.C.,
RA Shah P.P., Jain R., Joyce E.F., Capelson M.;
RT "Core Components of the Nuclear Pore Bind Distinct States of Chromatin and
RT Contribute to Polycomb Repression.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Plays a role in nuclear pore complex (NPC) assembly and
CC maintenance (PubMed:20547758). Required for nuclear import of Mad
CC (PubMed:20547758). Mediates the association between the nuclear pore
CC complex and a subset of active chromatin regions adjacent to lamin-
CC associated domains (PubMed:31784359). Plays a role in double strand
CC break repair by relocalizing the heterochromatic double strain breaks
CC (DSBs) to the nuclear periphery as part of the homologous recombination
CC (HR) repair process (PubMed:26502056). Regulates cytokinesis during
CC spermatocyte meiosis by maintaining type-B lamin Lam localization to
CC the spindle envelope (PubMed:27402967). Regulates female gonad
CC development and oogenesis (PubMed:26485283).
CC {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26485283,
CC ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:27402967,
CC ECO:0000269|PubMed:31784359}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC).
CC {ECO:0000250|UniProtKB:P57740}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:31784359}. Nucleus
CC envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:27402967}.
CC Nucleus membrane {ECO:0000269|PubMed:26485283}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18562695}. Chromosome
CC {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:31784359}. Nucleus
CC matrix {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
CC Note=Located on both the cytoplasmic and nuclear sides of the NPC core
CC structure (By similarity). During syncytial embryo and larval
CC neuroblast mitosis localizes to the nuclear envelope in interphase,
CC accumulates in the nucleus in prometaphase, localizes to the spindle
CC envelope in metaphase and then to condensing chromatin in telophase
CC (PubMed:18562695). In spermatocytes, detected in the nuclear matrix by
CC the nuclear envelope in metaphase I, and in the spindle envelope in
CC premeiotic nuclei and during anaphase I (PubMed:27402967). Colocalizes
CC with type-B lamin Lam throughout meiosis I (PubMed:27402967). Unlike in
CC mammals, does not localize to kinetochore (PubMed:18562695,
CC PubMed:27402967). Can localize to the nuclear lumen proximal to the
CC inner nuclear membrane (PubMed:31784359).
CC {ECO:0000250|UniProtKB:P57740, ECO:0000269|PubMed:18562695,
CC ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatocytes (at protein level).
CC {ECO:0000269|PubMed:27402967}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults (at
CC protein level) (PubMed:18562695, PubMed:31626769). Expressed in
CC embryonal and larval neuroblasts (at protein level) (PubMed:18562695).
CC Expressed during oogenesis (at protein level) (PubMed:31626769).
CC {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:31626769}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:18562695,
CC PubMed:26485283). RNAi-mediated knockdown in somatic gonadal cells
CC results in female, but not male, infertility associated with extensive
CC disintegration of the egg chambers and cell death in nurse cells
CC (PubMed:26485283). RNAi-mediated knockdown in spermatocytes causes
CC abnormal localization of nuclear type-B lamin Lam, abnormal spindle
CC envelope integrity and overall defective cytokinesis in meiosis
CC (PubMed:27402967). {ECO:0000269|PubMed:18562695,
CC ECO:0000269|PubMed:26485283, ECO:0000269|PubMed:27402967}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup84/Nup107 family.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF53002.1; -; Genomic_DNA.
DR EMBL; AF160938; AAD46878.1; -; mRNA.
DR RefSeq; NP_609446.1; NM_135602.4.
DR AlphaFoldDB; Q9V466; -.
DR SMR; Q9V466; -.
DR IntAct; Q9V466; 3.
DR STRING; 7227.FBpp0079710; -.
DR PaxDb; Q9V466; -.
DR DNASU; 34481; -.
DR EnsemblMetazoa; FBtr0080121; FBpp0079710; FBgn0027868.
DR GeneID; 34481; -.
DR KEGG; dme:Dmel_CG6743; -.
DR UCSC; CG6743-RA; d. melanogaster.
DR CTD; 57122; -.
DR FlyBase; FBgn0027868; Nup107.
DR VEuPathDB; VectorBase:FBgn0027868; -.
DR eggNOG; KOG1964; Eukaryota.
DR GeneTree; ENSGT00390000012080; -.
DR HOGENOM; CLU_012944_1_0_1; -.
DR InParanoid; Q9V466; -.
DR OMA; MAHIVLF; -.
DR OrthoDB; 671846at2759; -.
DR PhylomeDB; Q9V466; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9V466; -.
DR BioGRID-ORCS; 34481; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34481; -.
DR PRO; PR:Q9V466; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027868; Expressed in secondary oocyte and 30 other tissues.
DR ExpressionAtlas; Q9V466; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:FlyBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0030703; P:eggshell formation; IMP:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:UniProtKB.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:FlyBase.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048137; P:spermatocyte division; IMP:UniProtKB.
DR InterPro; IPR007252; Nup84/Nup107.
DR PANTHER; PTHR13003; PTHR13003; 1.
DR Pfam; PF04121; Nup84_Nup100; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..845
FT /note="Nuclear pore complex protein Nup107"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441254"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 364
FT /note="D->N: Reduced female fertility caused by perturbed
FT oogenesis which includes chorion defects and general
FT ovariole disintegration due to apoptosis."
FT /evidence="ECO:0000269|PubMed:26485283"
SQ SEQUENCE 845 AA; 97382 MW; 0A75B807A6AFD6B6 CRC64;
MADSPFPRSS RSGLLRTTLN SSMPPQNLSH SLLILEKSNA EQNELSLMED TGDDLDRGKS
RMDVLFPQFF DVLQAQGNGQ EAFEVIQSLT QVCRGVVEQL ELEIDHGMGG EQGARQRESM
LTWLRQEINT WRLLHALFYD RILLQTDRQA DDEMQDGPTL GGSEKEVIQQ LYALNATLRE
YQLVVDWLEA CYDRGEQQNP LHAHDRMMAW ENTLFQLENL QGAAFGKGHK IVTRLDPDAP
VREKRPLHAL DEEDNLRLSR AIFELIRAGR VDDGLKLCKH FGQTWRAAIL EGWRLHEDPN
FEQNVSVLHE KLPIEGNPRR DIWKRCAWML ADSKNYDEYS RATAGVFSGH LGSLKTLLHS
NWHDLLWAHL KVQIDIRVES EIRGCCLKNY QPMPDDYWNG RMTMEQIFEE LNVAKDASVR
DFAQSQLGII QRHLILDTCG ELIQHMVRWV EKDTSQQSPH QLRFMAHIVL FLRQIGRVEQ
ERQAEKIVAA YVEALIARGE PQLIAYYTAS LSNPLQVQLY SRFLEQVEQK RPRELAVDAA
LQAGLDVEQI TRVTVQNIRL AHQPLGEFGE PQSGEISAID QRKISALEWL IHLPEQRGEL
LWQANAMIRT YLASSKVECM RQTFRMVPAD IVQQLVSLYG SVDNIPPREE CCLKEYLCYK
AYLSGVDSFV EWNRLQQNRP KKPQTSHAAS SQDNFTERMA SERKEQAHRS EVVRWEHKVK
EQAKQTIELL YNVLMFPDKG WLVDPFIAKL PENAVQLSWD HRLLQMEKLR SICIPEIALF
LNEVMFKSGD FAGCVRLADE ISSENRQLYK VYTKHKLAEL LAKIADASLE LLNSKLDPWG
YPITT
